13 research outputs found
Synthesis and evaluation of a novel ionophore based on a thiacalix[4]arene derivative bearing imidazole units
In-vivo nuclear magnetic resonance studies for water quantification: Experimental and human applications
Copper(II) complexes of prion protein fragments; HuPrP(106-114), ChPrP(106-114) and related peptides
Pluralistic Approaches to Languages in the Curriculum:The Case of French-speaking Switzerland, Spain and Austria
Callyspongisines A–D: bromopyrrole alkaloids from an Australian marine sponge, Callyspongia sp.
Copper(II) Sequentially Loads onto the N-Terminal Amino Group of the Cellular Prion Protein before the Individual Octarepeats
The cellular prion protein (PrP<sup>C</sup>) binds to Cu<sup>2+</sup> ions <i>in vivo</i>,
and a misfolded form of PrP<sup>C</sup> is responsible for a range
of transmissible spongiform encephalopathies.
Recently, disruption of Cu<sup>2+</sup> homeostasis in mice has been
shown to impart resistance to scrapie infection. Using full-length
PrP<sup>C</sup> and model peptide fragments, we monitor the sequential
loading of Cu<sup>2+</sup> ions onto PrP<sup>C</sup> using visible
circular dichroism. We show the N-terminal amino group of PrP<sup>C</sup> is not the principal binding site for Cu<sup>2+</sup>; however,
surprisingly, it has an affinity for Cu<sup>2+</sup> tighter than
that of the individual octarepeat binding sites present within PrP<sup>C</sup>. We re-evaluate what is understood about the sequential loading
of Cu<sup>2+</sup> onto the full-length protein and show for the first
time that Cu<sup>2+</sup> loads onto the N-terminal amino group before
the single octarepeat binding sites